3H9H

Human Class I MHC HLA-A2(A150P) in complex with the Tel1p peptide

Summary for 3H9H

• Entry DOI: 10.2210/pdb3h9h/pdb
• Related: 1DUZ 3H7B 3H9S
• Descriptor: HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, Tel1p peptide, ... (5 entities in total)
• Functional Keywords: tel1p peptide, nonapeptide, mhc class i, hla-a2, tcr a6, cross-reactivity, disulfide bond, glycoprotein, host-virus interaction, immune response, membrane, mhc i, phosphoprotein, transmembrane, disease mutation, glycation, immunoglobulin domain, pyrrolidone carboxylic acid, secreted, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01892; Secreted . Note=(Microbial infection) In the presence of M: P61769
• Total number of polymer chains: 6
• Total formula weight: 90324.45

Authors

Borbulevych, O.Y.,Baker, B.M. (deposition date: 2009-04-30, release date: 2010-01-12, Last modification date: 2024-10-09)

Primary citation

Borbulevych, O.Y.,Piepenbrink, K.H.,Gloor, B.E.,Scott, D.R.,Sommese, R.F.,Cole, D.K.,Sewell, A.K.,Baker, B.M.
T cell receptor cross-reactivity directed by antigen-dependent tuning of peptide-MHC molecular flexibility.
Immunity, 31:885-896, 2009

PubMed Abstract: T cell-mediated immunity requires T cell receptor (TCR) cross-reactivity, the mechanisms behind which remain incompletely elucidated. The alphabeta TCR A6 recognizes both the Tax (LLFGYPVYV) and Tel1p (MLWGYLQYV) peptides presented by the human class I MHC molecule HLA-A2. Here we found that although the two ligands are ideal structural mimics, they form substantially different interfaces with A6, with conformational differences in the peptide, the TCR, and unexpectedly, the MHC molecule. The differences between the Tax and Tel1p ternary complexes could not be predicted from the free peptide-MHC structures and are inconsistent with a traditional induced-fit mechanism. Instead, the differences were attributable to peptide and MHC molecular motion present in Tel1p-HLA-A2 but absent in Tax-HLA-A2. Differential "tuning" of the dynamic properties of HLA-A2 by the Tax and Tel1p peptides thus facilitates cross-recognition and impacts how structural diversity can be presented to and accommodated by receptors of the immune system.

PubMed: 20064447
DOI: 10.1016/j.immuni.2009.11.003

Experimental method

X-RAY DIFFRACTION (2 Å)